[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=1719547 [NCBI, ExPASy, EBI, Israel, Japan] Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.; "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."; Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991).
[2]	X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 871-1090. DOI=10.1038/386247a0; PubMed=9069282 [NCBI, ExPASy, EBI, Israel, Japan] Zhang G., Liu Y., Ruoho A.E., Hurley J.H.; "Structure of the adenylyl cyclase catalytic core."; Nature 386:247-253(1997).
[3]	ERRATUM. Zhang G., Liu Y., Ruoho A.E., Hurley J.H.; Nature 388:204-204(1997).
[4]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA. DOI=10.1126/science.278.5345.1907; PubMed=9417641 [NCBI, ExPASy, EBI, Israel, Japan] Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.; "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."; Science 278:1907-1916(1997).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA. DOI=10.1126/science.285.5428.756; PubMed=10427002 [NCBI, ExPASy, EBI, Israel, Japan] Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.; "Two-metal-ion catalysis in adenylyl cyclase."; Science 285:756-760(1999).

Comments

FUNCTION: This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.
CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
ENZYME REGULATION: Insensitive to calcium/calmodulin. Stimulated by the G protein beta and gamma subunit complex.
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Expressed in brain and, at lower levels, in olfactory epithelium and lung.
SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
SIMILARITY: Contains 2 guanylate cyclase domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M80550; AAA40682.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A41541; A41541.

NP_112269.1; -.

3D structure databases

PDB

1AB8; X-ray; 2.20 A; A/B=871-1090.	[ExPASy / RCSB / EBI]
1AZS; X-ray; 2.30 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CJK; X-ray; 3.00 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CJT; X-ray; 2.80 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CJU; X-ray; 2.80 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CJV; X-ray; 3.00 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CS4; X-ray; 2.50 A; B=870-1081.	[ExPASy / RCSB / EBI]
1CUL; X-ray; 2.40 A; B=874-1081.	[ExPASy / RCSB / EBI]
1TL7; X-ray; 2.80 A; B=870-1081.	[ExPASy / RCSB / EBI]
1U0H; X-ray; 2.90 A; B=870-1081.	[ExPASy / RCSB / EBI]
2GVD; X-ray; 2.90 A; B=870-1081.	[ExPASy / RCSB / EBI]
2GVZ; X-ray; 3.27 A; B=870-1081.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AB8; -.
1AZS; -.
1CJK; -.
1CJT; -.
1CJU; -.
1CJV; -.
1CS4; -.
1CUL; -.
1TL7; -.
1U0H; -.
2GVD; -.
2GVZ; -.

ModBase

P26769.

Protein-protein interaction databases

DIP

DIP:164N; -.

PTM databases

PhosphoSite

P26769; -.

Organism-specific databases

RGD

619965; Adcy2.

Gene expression databases

ArrayExpress

P26769; -.

GermOnline

ENSRNOG00000032150; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0004016;	Molecular function: adenylate cyclase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006171;	Biological process: cAMP biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001054; A/G_cyclase.
IPR009398; Aden_cycl_like.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.1230; A/G_cyclase; 2.

Pfam

PF06327; DUF1053; 1.
PF00211; Guanylate_cyc; 2.
Pfam graphical view of domain structure.

SMART

SM00044; CYCc; 2.
SMART graphical view of domain structure.

PROSITE

PS00452; GUANYLATE_CYCLASE_1; 2.
PS50125; GUANYLATE_CYCLASE_2; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000032150; Rattus norvegicus. [Contig view]

GeneID

81636; -.

KEGG

rno:81636; -.

Phylogenomic databases

HOVERGEN

P26769; -.

Other

LinkHub

P26769; -.

NextBio

615124; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Repeat; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1090`	`1090`	`Adenylate cyclase type 2.`	`PRO_0000195686`
`TOPO_DOM`	`1 44`	`44`	`Cytoplasmic (Potential).`
`TRANSMEM`	`45 65`	`21`	`Potential.`
`TRANSMEM`	`75 95`	`21`	`Potential.`
`TRANSMEM`	`107 127`	`21`	`Potential.`
`TRANSMEM`	`132 152`	`21`	`Potential.`
`TRANSMEM`	`157 177`	`21`	`Potential.`
`TRANSMEM`	`186 206`	`21`	`Potential.`
`TOPO_DOM`	`207 600`	`394`	`Cytoplasmic (Potential).`
`TRANSMEM`	`601 621`	`21`	`Potential.`
`TRANSMEM`	`626 646`	`21`	`Potential.`
`TRANSMEM`	`679 699`	`21`	`Potential.`
`TRANSMEM`	`734 754`	`21`	`Potential.`
`TRANSMEM`	`763 783`	`21`	`Potential.`
`TRANSMEM`	`800 820`	`21`	`Potential.`
`TOPO_DOM`	`821 1090`	`270`	`Cytoplasmic (Potential).`
`METAL`	`294 294`		`Magnesium 1 (By similarity).`
`METAL`	`294 294`		`Magnesium 2 (By similarity).`
`METAL`	`295 295`		`Magnesium 2; via carbonyl oxygen (By similarity).`
`METAL`	`338 338`		`Magnesium 1 (By similarity).`
`METAL`	`338 338`		`Magnesium 2 (By similarity).`
`CARBOHYD`	`712 712`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`717 717`		`N-linked (GlcNAc...) (Potential).`
`STRAND`	`879 891`	`13`
`HELIX`	`895 898`	`4`
`TURN`	`903 908`	`6`
`HELIX`	`909 923`	`15`
`HELIX`	`924 927`	`4`
`HELIX`	`929 931`	`3`
`STRAND`	`934 940`	`7`
`STRAND`	`943 948`	`6`
`HELIX`	`967 987`	`21`
`TURN`	`988 991`	`4`
`STRAND`	`997 1010`	`14`
`STRAND`	`1012 1014`	`3`
`STRAND`	`1016 1021`	`6`
`HELIX`	`1022 1032`	`11`
`STRAND`	`1039 1041`	`3`
`HELIX`	`1043 1052`	`10`

Sequence information

Length: 1090 AA [This is the length of the unprocessed precursor]

Molecular weight: 123316 Da [This is the MW of the unprocessed precursor]

CRC64: 935CE44DF73199B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL LIVMGACLAL 

        70         80         90        100        110        120 
LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV FKKLLRVFSL VIWICLVAMG 

       130        140        150        160        170        180 
YLFMCFGGTV SAWDQVSFFL FIIFVVYTML PFNMRDAIIA SILTSSSHTI VLSVYLSATP 

       190        200        210        220        230        240 
GAKEHLFWQI LANVIIFICG NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE 

       250        260        270        280        290        300 
RLLLSLLPAH IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 

       310        320        330        340        350        360 
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL PNHAKNCVKM 

       370        380        390        400        410        420 
GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW QYDVWSHDVT LANHMEAGGV 

       430        440        450        460        470        480 
PGRVHISSVT LEHLNGAYKV EEGDGEIRDP YLKQHLVKTY FVINPKGERR SPQHLFRPRH 

       490        500        510        520        530        540 
TLDGAKMRAS VRMTRYLESW GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR 

       550        560        570        580        590        600 
TKSQKKRFEE ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 

       610        620        630        640        650        660 
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL LQCSKKASTS 

       670        680        690        700        710        720 
LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL SNSEETTLPT ANTSNANVSV 

       730        740        750        760        770        780 
PDNQASILHA RNLFFLPYFI YSCILGLISC SVFLRVNYEL KMLIMMVALV GYNTILLHTH 

       790        800        810        820        830        840 
AHVLDAYSQV LFQRPGIWKD LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE 

       850        860        870        880        890        900 
REEIETMENL NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 

       910        920        930        940        950        960 
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL SAIPSQEHAQ 

       970        980        990       1000       1010       1020 
EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI NHGPVIAGVI GAQKPQYDIW 

      1030       1040       1050       1060       1070       1080 
GNTVNVASRM DSTGVLDKIQ VTEETSLILQ TLGYTCTCRG IINVKGKGDL KTYFVNTEMS 

      1090 
RSLSQSNLAS

P26769 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools